Abstract
The histone-like protein HU isolated from Escherichia coli exhibited, after several purification steps, a Mg(2+)-dependent nuclease activity. We show here that this activity can be dissociated from HU by a denaturation-renaturation step, and is due to a small fraction of ribosomal protein S16 co-purifying with HU. S16 is an essential component of the 30S ribosomal particles. We have cloned, overproduced, and purified a histidine-tagged S16 and shown that this protein is a DNA-binding protein carrying a Mg(2+)-Mn(2+)-dependent endonuclease activity. This is an unexpected property for a ribosomal protein.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Bacterial Proteins / isolation & purification
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Base Sequence
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DNA Primers / genetics
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DNA, Bacterial / genetics
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DNA-Binding Proteins / isolation & purification
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Endonucleases / genetics
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Endonucleases / isolation & purification
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Endonucleases / metabolism*
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Escherichia coli / genetics
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Escherichia coli / metabolism*
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Magnesium / metabolism
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Manganese / metabolism
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Molecular Sequence Data
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Ribosomal Proteins / genetics
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Ribosomal Proteins / isolation & purification
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Ribosomal Proteins / metabolism*
Substances
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Bacterial Proteins
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DNA Primers
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DNA, Bacterial
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DNA-Binding Proteins
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Ribosomal Proteins
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histone-like protein HU, bacteria
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ribosomal protein S16
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Manganese
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Endonucleases
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Magnesium